Interaction of the α2A domain of integrin with small collagen fragments.
Siebert, Hans-Christian; Burg-Roderfeld, Monika; Eckert, Thomas; Stötzel, Sabine; Kirch, Ulrike; Diercks, Tammo; Humphries, Martin J; Frank, Martin; Wechselberger, Rainer; Tajkhorshid, Emad; Oesser, Steffen.
; 1(4): 393-405, 2010 Apr.
Artigo em Inglês | MEDLINE | ID: mdl-21203951
Unique Conformation in a Natural Interruption Sequence of Type XIX Collagen Revealed by Its High-Resolution Crystal Structure.
Fecal Excretion of Orally Administered Collagen-Like Peptides in Rats: Contribution of the Triple-Helical Conformation to Their Stability.
Changes in composition and content of food-derived peptide in human blood after daily ingestion of collagen hydrolysate for 4 weeks.
The structure of integrin α1I domain in complex with a collagen-mimetic peptide.
Non-linearity of the collagen triple helix in solution and implications for collagen function.
Integrin recognition motifs in the human collagens.
Benchmark reaction rates, the stability of biological molecules in water, and the evolution of catalytic power in enzymes.
Noncovalent Modulation of the Inverse Temperature Transition and Self-Assembly of Elastin-b-Collagen-like Peptide Bioconjugates.
Crystal structure of full-length human collagenase 3 (MMP-13) with peptides in the active site defines exosites in the catalytic domain.
Transmembrane collagen receptors.